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The nuclear envelope consists of two lipid bilayer membranes: an inner nuclear membrane and an outer nuclear membrane. [4] The space between the membranes is called the perinuclear space. It is usually about 10–50 nm wide. [5] [6] The outer nuclear membrane is continuous with the endoplasmic reticulum membrane. [4]
The nuclear pore complex (NPC), is a large protein complex giving rise to the nuclear pore. Nuclear pores are found in the nuclear envelope that surrounds the cell nucleus in eukaryotic cells . The nuclear envelope is studded by a great number of nuclear pores that give access to various molecules, to and from the nucleoplasm and the cytoplasm.
Within the perinuclear space (between inner and outer nuclear membranes) are SUN-1 and -2 which form connections with the KASH domain proteins on nesprin and the nuclear envelope lumen. [3] Interestingly, the removal of either SUN -1 or -2 individually will not disrupt LINC complex connectivity, indicating the similarity between the two proteins.
The outer nuclear membrane is continuous with the rough endoplasmic reticulum membrane, and like that structure, features ribosomes attached to the surface. The outer membrane is also continuous with the inner nuclear membrane since the two layers are fused together at numerous tiny holes called nuclear pores that perforate the nuclear envelope.
The inner membrane surrounds the nuclear content, providing its defining edge. [11]: 14 Embedded within the inner membrane, various proteins bind the intermediate filaments that give the nucleus its structure. [10]: 649 The outer membrane encloses the inner membrane, and is continuous with the adjacent endoplasmic reticulum membrane.
As with electrons in the electron shell model, protons in the outermost shell are relatively loosely bound to the nucleus if there are only few protons in that shell, because they are farthest from the center of the nucleus. Therefore, nuclei which have a full outer proton shell will be more tightly bound and have a higher binding energy than ...
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). [1] The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm.
They contain a C-terminal KASH transmembrane domain and are part of the LINC complex (Linker of Nucleoskeleton and Cytoskeleton) which is a protein network that associates the nuclear envelope (the membrane surrounding the nucleus) to the cytoskeleton, outside the nucleus, and the nuclear lamina, inside the nucleus.